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Related Concept Videos

Histone Modification02:32

Histone Modification

16.0K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Chromatin Packaging02:21

Chromatin Packaging

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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
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Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Updated: Jan 22, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

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Histone chaperone networks shaping chromatin function.

Colin M Hammond1, Caroline B Strømme1, Hongda Huang2

  • 1Biotech Research and Innovation Centre (BRIC) and Centre for Epigenetics, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen DK-2200, Denmark.

Nature Reviews. Molecular Cell Biology
|January 6, 2017
PubMed
Summary
This summary is machine-generated.

Histone chaperones are crucial for maintaining DNA integrity and gene expression by guiding histone assembly and epigenetic information. This review highlights their network and cooperative functions in cellular processes.

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In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Histone association with chaperone complexes is vital for histone folding, modification, nuclear import, and genomic localization.
  • Histone chaperoning impacts gene expression, chromosome segregation, and genome replication and repair.

Purpose of the Study:

  • To review the structural and functional properties of histone chaperones.
  • To emphasize the cooperative mechanisms within the histone chaperone network.

Main Methods:

  • Review of existing literature on histone chaperones and their complexes.
  • Analysis of structural and functional data related to histone-chaperone interactions.

Main Results:

  • The histone chaperone network comprises distinct structural and functional entities.
  • Chaperones cooperate through networks and co-chaperone complexes to regulate histone supply and demand.
  • This cooperation ensures proper nucleosome assembly and maintains epigenetic information.

Conclusions:

  • Histone chaperones are essential regulators of fundamental chromosomal processes.
  • Cooperative interactions within the histone chaperone network are critical for maintaining genome stability and epigenetic fidelity.